#Question id: 863
#Part-B Specialized Branches in Biotechnology
Ubiquitinated proteins are proteolytically degraded in an ATP-dependent process mediated by a large (∼2500 kD, 26S) multiprotein complex named the 26S proteasome;
#Question id: 865
#Part-B Specialized Branches in Biotechnology
In autophagy, the endoplasmic reticulum (ER) first gives rise to a cup-shaped, membranous cisterna called the______
#Question id: 869
#Part-B Specialized Branches in Biotechnology
Which statements are correct regarding protein folding
A. Many molecular chaperones were first described as heat shock proteins (Hsp) because Their rate of synthesis is increased at elevated temperatures
B. The renaturation of a denatured protein in vitro may not entirely mimic the folding of a protein in vivo.
C. Molecular chaperones are essential proteins that bind to only partially folded polypeptide chains.
D. Molecular chaperones function to lift folding polypeptides out of the false minima in their folding funnel.
#Question id: 872
#Part-B Specialized Branches in Biotechnology
Which of the following statements is not true about HSP 70 family.
A. They have a molecular weight near 70,000 and are abundant in cells stressed by elevated temperature.
B. Bind to regions of unfolded polypeptides that are rich in hydrophilic residues
C. Hsp70 proteins not block the folding of certain proteins that must remain unfolded untill they have been translocated across a membrane.
D.) It releases polypeptides in a cycle that uses energy from ATP hydrolysis.
#Question id: 875
#Part-B Specialized Branches in Biotechnology
Why positive phi angles less common than negative Phi angles in proteins contain L amino acid?
#Question id: 877
#Part-B Specialized Branches in Biotechnology
The sharp transition seen in Figure suggests that
A. Proteins can be denatured by any treatment that disrupts the weak bonds stabilizing tertiary structure, such as heating, or by chemical denaturants such as urea or guanidinium chloride.
B. A comparison of the degree of unfolding as the concentration of denaturant increases reveals a sharp transition from the folded, or native, form to the unfolded, or denatured form, suggesting that only these two conformational states are present to any significant extent.
C. A similar sharp transition is observed if denaturants are removed from unfolded proteins, allowing the proteins to fold.
D. Protein folding and unfolding is an “all or none” process that results from a cooperative transition .